Please use this identifier to cite or link to this item: http://hdl.handle.net/10603/3232
Title: Vaccinia virus complement control protein VCP structure function analysis and role in vaccinia virus pathogenesis
Researcher: Ahmad, Muzammil
Guide(s): Sahu, Arvind
Keywords: Cell sciences
VCP
Vaccinia virus
Upload Date: 4-Nov-2011
University: University of Pune
Completed Date: November, 2010
Abstract: The complement system is a principal component of innate immunity designed to combat a myriad of existing as well as newly emerging pathogens. Since viruses are obligatory intracellular parasites, they are continuously exposed to host complement assault and therefore, not surprisingly, have imbibed various strategies to subvert it. One of them is molecular mimicry of the host complement regulators and the examples are pox and herpesviruses, which encode proteins that are structurally and functionally similar to the human regulators of complement activation (RCA), a family of proteins that regulate complement. Vaccinia virus (VACV) is the most extensively studied member of poxviruses. It encodes a homolog of the human complement regulators named vaccinia virus complement control protein (VCP). Incidentally, it is also the most studied viral RCA molecule whose complete structure is determined. This four complement control protein domain containing secretory protein is known to inhibit complement activation by supporting the factor I-mediated inactivation of complement proteins C3b and C4b (termed cofactor activity; CFA), and by accelerating the irreversible decay of the classical and to a limited extent of the alternative pathway C3-convertases (termed decayaccelerating activity; DAA). Here, I have mapped the VCP domains important for its CFA and DAA by swapping its individual domains with those of the human decayaccelerating factor (DAF; CD55) and membrane cofactor protein (MCP; CD46). We reasoned that since DAF possesses only decay activity and is devoid of cofactor activity, while MCP possesses only cofactor activity and is devoid of decay activity, swapping of VCP domains with homologous DAF or MCP domains would allow the identification of VCP domains(s) critical for factor I interaction and decay of protease subunits from the convertases, respectively.
Pagination: x, 156p.
URI: http://hdl.handle.net/10603/3232
Appears in Departments:National Centre for Cell Science

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01_title.pdfAttached File22.55 kBAdobe PDFView/Open
02_declaration.pdf32.62 kBAdobe PDFView/Open
03_table of contents.pdf102.82 kBAdobe PDFView/Open
04_acknowledgements.pdf69.59 kBAdobe PDFView/Open
05_list of symbols & abbreviations.pdf55.31 kBAdobe PDFView/Open
06_abstract.pdf82.32 kBAdobe PDFView/Open
07_chapter 1.pdf1.76 MBAdobe PDFView/Open
08_chapter 2.pdf1.84 MBAdobe PDFView/Open
09_chapter 3.pdf1.49 MBAdobe PDFView/Open
10_chapter 4.pdf788.09 kBAdobe PDFView/Open
11_references.pdf222.62 kBAdobe PDFView/Open
12_publications.pdf1.05 MBAdobe PDFView/Open


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